SMOX

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Spermine oxidase
Identifiers
Symbol(s) SMOX; SMO; C20orf16; FLJ20746; MGC1010; PAO; PAOh1; dJ779E11.1
External IDs MGI: 2445356 HomoloGene: 69268
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 54498 228608
Ensembl ENSG00000088826 ENSMUSG00000027333
Uniprot Q9NWM0 Q3UPW5
Refseq NM_175839 (mRNA)
NP_787033 (protein)		 NM_145533 (mRNA)
NP_663508 (protein)
Location Chr 20: 4.08 - 4.12 Mb Chr 2: 131.18 - 131.22 Mb
Pubmed search [1] [2]

Spermine oxidase, also known as SMOX, is a human gene.[1]

The product of this gene is the polyamine oxidase. This enzyme potentially represents a new class of catabolic enzymes in the mammalian polyamine metabolic pathway capable of the efficient oxidation of polyamines. More than five transcript variants encoding four active isoenzymes have been identified for this gene, however, not all variants have been fully described. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism.[1]

[edit] References

  1. ^ a b Entrez Gene: SMOX spermine oxidase.

[edit] Further reading

  • Seiler N (2005). "Catabolism of polyamines.". Amino Acids 26 (3): 217–33. doi:10.1007/s00726-004-0070-z. PMID 15221502. 
  • Hölttä E (1977). "Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase.". Biochemistry 16 (1): 91–100. PMID 12798. 
  • Tsukada T, Furusako S, Maekawa S, et al. (1988). "Purification by affinity chromatography and characterization of porcine liver cytoplasmic polyamine oxidase.". Int. J. Biochem. 20 (7): 695–702. PMID 3181599. 
  • Wang Y, Devereux W, Woster PM, et al. (2001). "Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure.". Cancer Res. 61 (14): 5370–3. PMID 11454677. 
  • Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052. 
  • Vujcic S, Diegelman P, Bacchi CJ, et al. (2002). "Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin.". Biochem. J. 367 (Pt 3): 665–75. doi:10.1042/BJ20020720. PMID 12141946. 
  • Murray-Stewart T, Wang Y, Devereux W, Casero RA (2003). "Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics.". Biochem. J. 368 (Pt 3): 673–7. doi:10.1042/BJ20021587. PMID 12398765. 
  • Cervelli M, Polticelli F, Federico R, Mariottini P (2003). "Heterologous expression and characterization of mouse spermine oxidase.". J. Biol. Chem. 278 (7): 5271–6. doi:10.1074/jbc.M207888200. PMID 12458219. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Wang Y, Murray-Stewart T, Devereux W, et al. (2003). "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO.". Biochem. Biophys. Res. Commun. 304 (4): 605–11. PMID 12727196. 
  • Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Cervelli M, Bellini A, Bianchi M, et al. (2004). "Mouse spermine oxidase gene splice variants. Nuclear subcellular localization of a novel active isoform.". Eur. J. Biochem. 271 (4): 760–70. PMID 14764092. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Pledgie A, Huang Y, Hacker A, et al. (2006). "Spermine oxidase SMO(PAOh1), Not N1-acetylpolyamine oxidase PAO, is the primary source of cytotoxic H2O2 in polyamine analogue-treated human breast cancer cell lines.". J. Biol. Chem. 280 (48): 39843–51. doi:10.1074/jbc.M508177200. PMID 16207710. 
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